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Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP
Because of its unusual length, nascent thyroglobulin (Tg) requires a long time after translocation into the endoplasmic reticulum (ER) to assume its mature tertiary structure. Thus, Tg is an ideal molecule for the study of protein folding and export from the ER, and is an excellent potential substra...
Tallennettuna:
| Aineistotyyppi: | Artigo |
|---|---|
| Kieli: | Inglês |
| Julkaistu: |
The Rockefeller University Press
1992
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2289550/ https://ncbi.nlm.nih.gov/pubmed/1353499 |
| Tagit: |
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